GenomeNet

Database: PDB
Entry: 2IRU
LinkDB: 2IRU
Original site: 2IRU 
HEADER    TRANSFERASE                             16-OCT-06   2IRU              
TITLE     CRYSTAL STRUCTURE OF THE POLYMERASE DOMAIN FROM MYCOBACTERIUM         
TITLE    2 TUBERCULOSIS LIGASE D                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE DNA LIGASE-LIKE PROTEIN RV0938/MT0965;            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LIGD POLYMERASE DOMAIN (RESIDUES 1-300);                   
COMPND   5 EC: 2.7.7.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: RV098;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    POLYMERASE, PRIMASE, LIGASE, NHEJ, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.C.BRISSETT,R.S.PITCHER,A.J.DOHERTY                                  
REVDAT   4   13-JUL-11 2IRU    1       VERSN                                    
REVDAT   3   24-FEB-09 2IRU    1       VERSN                                    
REVDAT   2   30-OCT-07 2IRU    1       JRNL                                     
REVDAT   1   02-JAN-07 2IRU    0                                                
JRNL        AUTH   R.S.PITCHER,N.C.BRISSETT,A.J.PICHER,P.ANDRADE,R.JUAREZ,      
JRNL        AUTH 2 D.THOMPSON,G.C.FOX,L.BLANCO,A.J.DOHERTY                      
JRNL        TITL   STRUCTURE AND FUNCTION OF A MYCOBACTERIAL NHEJ DNA REPAIR    
JRNL        TITL 2 POLYMERASE.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 366   391 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17174332                                                     
JRNL        DOI    10.1016/J.JMB.2006.10.046                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 60313                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3237                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3268                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 192                          
REMARK   3   BIN FREE R VALUE                    : 0.4670                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4344                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 663                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 20.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.65000                                              
REMARK   3    B22 (A**2) : -0.21000                                             
REMARK   3    B33 (A**2) : -0.45000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.12000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.117         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.120         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.540         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4444 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6069 ; 1.478 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   566 ; 6.097 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   181 ;30.814 ;22.597       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   698 ;13.589 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    42 ;19.880 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   700 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3380 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2267 ; 0.215 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3055 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   479 ; 0.260 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    46 ; 0.198 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    23 ; 0.247 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2907 ; 0.924 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4579 ; 1.430 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1754 ; 2.269 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1490 ; 3.382 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     6        A   114                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9560  43.6160  21.8590              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0263 T22:   0.0267                                     
REMARK   3      T33:   0.0359 T12:  -0.0048                                     
REMARK   3      T13:  -0.0022 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7723 L22:   0.9954                                     
REMARK   3      L33:   1.3342 L12:   0.0915                                     
REMARK   3      L13:   0.1683 L23:   0.2552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0119 S12:   0.0165 S13:  -0.0467                       
REMARK   3      S21:  -0.1016 S22:  -0.0107 S23:   0.0177                       
REMARK   3      S31:   0.0220 S32:  -0.0859 S33:   0.0225                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   115        A   208                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.9670  22.0650  32.9130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1261 T22:  -0.0189                                     
REMARK   3      T33:   0.0374 T12:  -0.0205                                     
REMARK   3      T13:  -0.0230 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3809 L22:   1.4390                                     
REMARK   3      L33:   2.3692 L12:   0.3404                                     
REMARK   3      L13:   0.0722 L23:  -1.4353                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0451 S12:  -0.0488 S13:  -0.1058                       
REMARK   3      S21:  -0.1330 S22:  -0.0107 S23:  -0.0710                       
REMARK   3      S31:   0.4484 S32:  -0.0866 S33:  -0.0344                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   209        A   261                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3180  29.6690  39.4370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0783 T22:   0.0387                                     
REMARK   3      T33:   0.0059 T12:  -0.0425                                     
REMARK   3      T13:  -0.0233 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1869 L22:   1.3638                                     
REMARK   3      L33:   1.0002 L12:  -0.0450                                     
REMARK   3      L13:  -0.0830 L23:  -1.1216                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0218 S12:  -0.1082 S13:  -0.0098                       
REMARK   3      S21:   0.1396 S22:   0.0869 S23:   0.0904                       
REMARK   3      S31:   0.1171 S32:  -0.2243 S33:  -0.1087                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   262        A   291                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8030  34.2470  37.1140              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0105 T22:   0.0015                                     
REMARK   3      T33:   0.0108 T12:   0.0145                                     
REMARK   3      T13:  -0.0532 T23:   0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2355 L22:   2.9856                                     
REMARK   3      L33:   1.2636 L12:   1.0968                                     
REMARK   3      L13:   0.6539 L23:  -0.2056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1135 S12:  -0.3510 S13:  -0.2024                       
REMARK   3      S21:   0.2722 S22:  -0.0844 S23:  -0.3848                       
REMARK   3      S31:   0.1560 S32:   0.1365 S33:  -0.0291                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    10        B   115                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3600  59.6000  25.1050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0156 T22:   0.0314                                     
REMARK   3      T33:   0.0311 T12:  -0.0231                                     
REMARK   3      T13:  -0.0074 T23:   0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6343 L22:   1.1062                                     
REMARK   3      L33:   1.3674 L12:  -0.0205                                     
REMARK   3      L13:  -0.0430 L23:   0.2140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0231 S12:  -0.0683 S13:   0.0281                       
REMARK   3      S21:   0.1008 S22:  -0.0560 S23:   0.0815                       
REMARK   3      S31:  -0.0440 S32:  -0.0307 S33:   0.0328                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   116        B   162                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1900  78.9110  17.6130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1291 T22:   0.0243                                     
REMARK   3      T33:   0.0700 T12:  -0.0359                                     
REMARK   3      T13:  -0.0104 T23:  -0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5307 L22:   2.1878                                     
REMARK   3      L33:   4.3759 L12:  -0.1315                                     
REMARK   3      L13:  -0.1748 L23:  -1.8199                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0709 S12:   0.0450 S13:   0.0378                       
REMARK   3      S21:   0.1115 S22:  -0.0625 S23:   0.0138                       
REMARK   3      S31:  -0.2475 S32:   0.1492 S33:  -0.0084                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   163        B   190                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2290  81.1390  15.4280              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1237 T22:   0.0088                                     
REMARK   3      T33:   0.0102 T12:  -0.0957                                     
REMARK   3      T13:  -0.0032 T23:   0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5418 L22:   8.1237                                     
REMARK   3      L33:   1.6953 L12:  -1.1504                                     
REMARK   3      L13:  -0.2552 L23:   1.2260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0311 S12:  -0.0574 S13:   0.1298                       
REMARK   3      S21:   0.1693 S22:  -0.0798 S23:  -0.0695                       
REMARK   3      S31:  -0.3700 S32:   0.0929 S33:   0.0487                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   191        B   223                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.0090  85.4810   8.0680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0704 T22:   0.0002                                     
REMARK   3      T33:   0.0159 T12:   0.0166                                     
REMARK   3      T13:   0.0180 T23:   0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9026 L22:   1.7663                                     
REMARK   3      L33:  14.6893 L12:  -0.2002                                     
REMARK   3      L13:  -0.0057 L23:  -2.8035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0310 S12:   0.1191 S13:   0.0743                       
REMARK   3      S21:   0.1811 S22:   0.1854 S23:   0.1968                       
REMARK   3      S31:   0.0138 S32:  -0.6701 S33:  -0.2164                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   224        B   291                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7180  70.3430  12.1320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0222 T22:   0.0296                                     
REMARK   3      T33:   0.0040 T12:  -0.0425                                     
REMARK   3      T13:   0.0029 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8095 L22:   1.4151                                     
REMARK   3      L33:   1.4580 L12:  -0.6366                                     
REMARK   3      L13:   0.1336 L23:  -0.3322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0481 S12:   0.1232 S13:   0.0829                       
REMARK   3      S21:  -0.1138 S22:  -0.0853 S23:  -0.1147                       
REMARK   3      S31:  -0.1779 S32:   0.1724 S33:   0.0372                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2IRU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039937.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54180                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63571                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.700                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.1                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : 0.02900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.23500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.12900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M MG ACETATE, PH       
REMARK 280  7.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 285K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       37.89800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     MET A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     ALA A   292                                                      
REMARK 465     ASP A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     PRO A   295                                                      
REMARK 465     VAL A   296                                                      
REMARK 465     ALA A   297                                                      
REMARK 465     ASP A   298                                                      
REMARK 465     ARG A   299                                                      
REMARK 465     LEU A   300                                                      
REMARK 465     THR A   301                                                      
REMARK 465     ARG A   302                                                      
REMARK 465     TYR A   303                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     MET B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     SER B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     ALA B   292                                                      
REMARK 465     ASP B   293                                                      
REMARK 465     ALA B   294                                                      
REMARK 465     PRO B   295                                                      
REMARK 465     VAL B   296                                                      
REMARK 465     ALA B   297                                                      
REMARK 465     ASP B   298                                                      
REMARK 465     ARG B   299                                                      
REMARK 465     LEU B   300                                                      
REMARK 465     THR B   301                                                      
REMARK 465     ARG B   302                                                      
REMARK 465     TYR B   303                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CE   LYS B    55     O    HOH B   496              1.94            
REMARK 500   NH1  ARG A    11     O    HOH A   525              2.10            
REMARK 500   O    PRO B   189     O    HOH B   601              2.13            
REMARK 500   O    HOH B   513     O    HOH B   555              2.14            
REMARK 500   CD   ARG B   160     O    HOH B   495              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   487     O    HOH B   359     1655     2.03            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  54   CG  -  CD  -  NE  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    ARG B  54   CD  -  NE  -  CZ  ANGL. DEV. =  12.6 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ARG B  54   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  97       15.77   -144.02                                   
REMARK 500    SER A 177      -94.62   -107.24                                   
REMARK 500    LYS A 178      -33.70   -133.66                                   
REMARK 500    THR A 219      107.42    -23.67                                   
REMARK 500    TYR A 244       -7.01     74.20                                   
REMARK 500    SER B  88      -72.58    -71.31                                   
REMARK 500    ASP B  97       17.79   -146.08                                   
REMARK 500    SER B 177     -105.92   -106.34                                   
REMARK 500    THR B 219      133.53    -39.20                                   
REMARK 500    TYR B 244       -5.64     75.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 427        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A 474        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A 514        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH B 447        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH B 471        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH B 570        DISTANCE =  5.11 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IRX   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH GTP.                                 
REMARK 900 RELATED ID: 2IRY   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN COMPLEXED WITH DGTP.                                
DBREF  2IRU A    4   303  UNP    P71571   Y938_MYCTU       1    300             
DBREF  2IRU B    4   303  UNP    P71571   Y938_MYCTU       1    300             
SEQADV 2IRU GLY A    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRU SER A    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRU HIS A    3  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRU GLY B    1  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRU SER B    2  UNP  P71571              EXPRESSION TAG                 
SEQADV 2IRU HIS B    3  UNP  P71571              EXPRESSION TAG                 
SEQRES   1 A  303  GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR          
SEQRES   2 A  303  LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY          
SEQRES   3 A  303  THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL          
SEQRES   4 A  303  ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA          
SEQRES   5 A  303  THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA          
SEQRES   6 A  303  PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP          
SEQRES   7 A  303  LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR          
SEQRES   8 A  303  THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP          
SEQRES   9 A  303  ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN          
SEQRES  10 A  303  TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN          
SEQRES  11 A  303  PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO          
SEQRES  12 A  303  GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA          
SEQRES  13 A  303  ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL          
SEQRES  14 A  303  THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU          
SEQRES  15 A  303  TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA          
SEQRES  16 A  303  THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN          
SEQRES  17 A  303  ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER          
SEQRES  18 A  303  LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN          
SEQRES  19 A  303  SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG          
SEQRES  20 A  303  GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP          
SEQRES  21 A  303  ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR          
SEQRES  22 A  303  ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU          
SEQRES  23 A  303  LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG          
SEQRES  24 A  303  LEU THR ARG TYR                                              
SEQRES   1 B  303  GLY SER HIS MET GLY SER ALA SER GLU GLN ARG VAL THR          
SEQRES   2 B  303  LEU THR ASN ALA ASP LYS VAL LEU TYR PRO ALA THR GLY          
SEQRES   3 B  303  THR THR LYS SER ASP ILE PHE ASP TYR TYR ALA GLY VAL          
SEQRES   4 B  303  ALA GLU VAL MET LEU GLY HIS ILE ALA GLY ARG PRO ALA          
SEQRES   5 B  303  THR ARG LYS ARG TRP PRO ASN GLY VAL ASP GLN PRO ALA          
SEQRES   6 B  303  PHE PHE GLU LYS GLN LEU ALA LEU SER ALA PRO PRO TRP          
SEQRES   7 B  303  LEU SER ARG ALA THR VAL ALA HIS ARG SER GLY THR THR          
SEQRES   8 B  303  THR TYR PRO ILE ILE ASP SER ALA THR GLY LEU ALA TRP          
SEQRES   9 B  303  ILE ALA GLN GLN ALA ALA LEU GLU VAL HIS VAL PRO GLN          
SEQRES  10 B  303  TRP ARG PHE VAL ALA GLU PRO GLY SER GLY GLU LEU ASN          
SEQRES  11 B  303  PRO GLY PRO ALA THR ARG LEU VAL PHE ASP LEU ASP PRO          
SEQRES  12 B  303  GLY GLU GLY VAL MET MET ALA GLN LEU ALA GLU VAL ALA          
SEQRES  13 B  303  ARG ALA VAL ARG ASP LEU LEU ALA ASP ILE GLY LEU VAL          
SEQRES  14 B  303  THR PHE PRO VAL THR SER GLY SER LYS GLY LEU HIS LEU          
SEQRES  15 B  303  TYR THR PRO LEU ASP GLU PRO VAL SER SER ARG GLY ALA          
SEQRES  16 B  303  THR VAL LEU ALA LYS ARG VAL ALA GLN ARG LEU GLU GLN          
SEQRES  17 B  303  ALA MET PRO ALA LEU VAL THR SER THR MET THR LYS SER          
SEQRES  18 B  303  LEU ARG ALA GLY LYS VAL PHE VAL ASP TRP SER GLN ASN          
SEQRES  19 B  303  SER GLY SER LYS THR THR ILE ALA PRO TYR SER LEU ARG          
SEQRES  20 B  303  GLY ARG THR HIS PRO THR VAL ALA ALA PRO ARG THR TRP          
SEQRES  21 B  303  ALA GLU LEU ASP ASP PRO ALA LEU ARG GLN LEU SER TYR          
SEQRES  22 B  303  ASP GLU VAL LEU THR ARG ILE ALA ARG ASP GLY ASP LEU          
SEQRES  23 B  303  LEU GLU ARG LEU ASP ALA ASP ALA PRO VAL ALA ASP ARG          
SEQRES  24 B  303  LEU THR ARG TYR                                              
FORMUL   3  HOH   *663(H2 O)                                                    
HELIX    1   1 THR A   28  ALA A   48  1                                  21    
HELIX    2   2 SER A   98  GLN A  108  1                                  11    
HELIX    3   3 MET A  148  ASP A  165  1                                  18    
HELIX    4   4 SER A  191  MET A  210  1                                  20    
HELIX    5   5 THR A  219  ARG A  223  5                                   5    
HELIX    6   6 TRP A  231  SER A  235  5                                   5    
HELIX    7   7 THR A  259  ASP A  264  1                                   6    
HELIX    8   8 TYR A  273  GLY A  284  1                                  12    
HELIX    9   9 THR B   28  ALA B   48  1                                  21    
HELIX   10  10 SER B   98  GLN B  108  1                                  11    
HELIX   11  11 MET B  148  ILE B  166  1                                  19    
HELIX   12  12 SER B  191  MET B  210  1                                  20    
HELIX   13  13 TRP B  231  SER B  235  5                                   5    
HELIX   14  14 THR B  259  ASP B  265  1                                   7    
HELIX   15  15 SER B  272  GLY B  284  1                                  13    
SHEET    1   A 4 PHE A  66  GLU A  68  0                                        
SHEET    2   A 4 THR A  53  ARG A  56 -1  N  ARG A  56   O  PHE A  66           
SHEET    3   A 4 GLU A 112  VAL A 115 -1  O  HIS A 114   N  THR A  53           
SHEET    4   A 4 THR A 240  ILE A 241 -1  O  THR A 240   N  VAL A 115           
SHEET    1   B 2 SER A  80  VAL A  84  0                                        
SHEET    2   B 2 THR A  91  ILE A  95 -1  O  THR A  91   N  VAL A  84           
SHEET    1   C 4 TRP A 118  ALA A 122  0                                        
SHEET    2   C 4 LEU A 129  PRO A 143 -1  O  ASN A 130   N  VAL A 121           
SHEET    3   C 4 VAL A 227  ASP A 230 -1  O  ASP A 230   N  ASP A 140           
SHEET    4   C 4 VAL A 214  THR A 215  1  N  THR A 215   O  VAL A 229           
SHEET    1   D 5 TRP A 118  ALA A 122  0                                        
SHEET    2   D 5 LEU A 129  PRO A 143 -1  O  ASN A 130   N  VAL A 121           
SHEET    3   D 5 LEU A 180  VAL A 190 -1  O  LEU A 180   N  LEU A 141           
SHEET    4   D 5 PHE A 171  THR A 174 -1  N  VAL A 173   O  HIS A 181           
SHEET    5   D 5 ALA A 256  PRO A 257 -1  O  ALA A 256   N  THR A 174           
SHEET    1   E 2 THR A 253  VAL A 254  0                                        
SHEET    2   E 2 LEU A 271  SER A 272 -1  O  LEU A 271   N  VAL A 254           
SHEET    1   F 4 PHE B  66  GLU B  68  0                                        
SHEET    2   F 4 THR B  53  ARG B  56 -1  N  ARG B  54   O  GLU B  68           
SHEET    3   F 4 GLU B 112  VAL B 115 -1  O  HIS B 114   N  THR B  53           
SHEET    4   F 4 THR B 240  ILE B 241 -1  O  THR B 240   N  VAL B 115           
SHEET    1   G 2 SER B  80  ALA B  85  0                                        
SHEET    2   G 2 THR B  90  ILE B  95 -1  O  THR B  91   N  VAL B  84           
SHEET    1   H 4 TRP B 118  ALA B 122  0                                        
SHEET    2   H 4 LEU B 129  PRO B 143 -1  O  ASN B 130   N  VAL B 121           
SHEET    3   H 4 VAL B 227  ASP B 230 -1  O  PHE B 228   N  ASP B 142           
SHEET    4   H 4 VAL B 214  THR B 215  1  N  THR B 215   O  VAL B 229           
SHEET    1   I 5 TRP B 118  ALA B 122  0                                        
SHEET    2   I 5 LEU B 129  PRO B 143 -1  O  ASN B 130   N  VAL B 121           
SHEET    3   I 5 LEU B 180  VAL B 190 -1  O  LEU B 180   N  LEU B 141           
SHEET    4   I 5 PHE B 171  THR B 174 -1  N  VAL B 173   O  HIS B 181           
SHEET    5   I 5 ALA B 256  PRO B 257 -1  O  ALA B 256   N  THR B 174           
CRYST1   41.053   75.796   96.100  90.00  92.68  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.024359  0.000000  0.001142        0.00000                         
SCALE2      0.000000  0.013193  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010417        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system